MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it Structural basis for the nuclear export activity of Importin13. Structural basis for the nuclear export activity of Importin13. EMBO J. (0261-4189) 2013 imex curation Grünwald M., Lazzaretti D., Bono F. fulvia.bono@tuebingen.mpg.de 21-Jul-2014: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro thermal shift thermal shift binding thermal shift predetermined predetermined participant predetermined Grünwald M., Lazzaretti D., Bono F. fulvia.bono@tuebingen.mpg.de Accepted 2014-JUL-15 by MARTA EMBO J. (0261-4189) 2013 Only protein-protein interactions imex curation Structural basis for the nuclear export activity of Importin13. Structural basis for the nuclear export activity of Importin13. EMBO J. (0261-4189) 2013 imex curation Grünwald M., Lazzaretti D., Bono F. fulvia.bono@tuebingen.mpg.de 21-Jul-2014: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Grünwald M., Lazzaretti D., Bono F. fulvia.bono@tuebingen.mpg.de Accepted 2014-JUL-15 by MARTA EMBO J. (0261-4189) 2013 Only protein-protein interactions imex curation Structural basis for the nuclear export activity of Importin13. Structural basis for the nuclear export activity of Importin13. EMBO J. (0261-4189) 2013 imex curation Grünwald M., Lazzaretti D., Bono F. fulvia.bono@tuebingen.mpg.de 21-Jul-2014: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro pull down pull down weight by comassie molecular weight estimation by coomasie staining weight by comassie Grünwald M., Lazzaretti D., Bono F. fulvia.bono@tuebingen.mpg.de Accepted 2014-JUL-15 by MARTA EMBO J. (0261-4189) 2013 Only protein-protein interactions imex curation Structural basis for the nuclear export activity of Importin13. Structural basis for the nuclear export activity of Importin13. EMBO J. (0261-4189) 2013 imex curation Grünwald M., Lazzaretti D., Bono F. fulvia.bono@tuebingen.mpg.de 21-Jul-2014: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column weight by comassie molecular weight estimation by coomasie staining weight by comassie Grünwald M., Lazzaretti D., Bono F. fulvia.bono@tuebingen.mpg.de Accepted 2014-JUL-15 by MARTA EMBO J. (0261-4189) 2013 Only protein-protein interactions imex curation ipo13_human Importin-13 Ran-binding protein 13 Karyopherin-13 IPO13 KIAA0724 RANBP13 protein protein human Homo sapiens Human MERREEQPGAAGAGAAPALDFTVENVEKALHQLYYDPNIENKNLAQKWLMQAQVSPQAWHFSWQLLQPDKVPEIQYFGASALHIKISRYWSDIPTDQYESLKAQLFTQITRFASGSKIVLTRLCVALASLALSMMPDAWPCAVADMVRLFQAEDSPVDGQGRCLALLELLTVLPEEFQTSRLPQYRKGLVRTSLAVECGAVFPLLEQLLQQPSSPSCVRQKVLKCFSSWVQLEVPLQDCEALIQAAFAALQDSELFDSSVEAIVNAISQPDAQRYVNTLLKLIPLVLGLQEQLRQAVQNGDMETSHGICRIAVALGENHSRALLDQVEHWQSFLALVNMIMFCTGIPGHYPVNETTSSLTLTFWYTLQDDILSFEAEKQAVYQQVYRPVYFQLVDVLLHKAQFPSDEEYGFWSSDEKEQFRIYRVDISDTLMYVYEMLGAELLSNLYDKLGRLLTSSEEPYSWQHTEALLYGFQSIAETIDVNYSDVVPGLIGLIPRISISNVQLADTVMFTIGALSEWLADHPVMINSVLPLVLHALGNPELSVSSVSTLKKICRECKYDLPPYAANIVAVSQDVLMKQIHKTSQCMWLMQALGFLLSALQVEEILKNLHSLISPYIQQLEKLAEEIPNPSNKLAIVHILGLLSNLFTTLDISHHEDDHEGPELRKLPVPQGPNPVVVVLQQVFQLIQKVLSKWLNDAQVVEAVCAIFEKSVKTLLDDFAPMVPQLCEMLGRMYSTIPQASALDLTRQLVHIFAHEPAHFPPIEALFLLVTSVTLTLFQQGPRDHPDIVDSFMQLLAQALKRKPDLFLCERLDVKAVFQCAVLALKFPEAPTVKASCGFFTELLPRCGEVESVGKVVQEDGRMLLIAVLEAIGGQASRSLMDCFADILFALNKHCFSLLSMWIKEALQPPGFPSARLSPEQKDTFSQQILRERVNKRRVKEMVKEFTLLCRGLHGTDYTADY 8C696EE2B92365F0 ran_human GTP-binding nuclear protein Ran GTPase Ran Ras-related nuclear protein Ras-like protein TC4 Androgen receptor-associated protein 24 RAN ARA24 OK/SW-cl.81 protein protein human Homo sapiens Human MAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIKFNVWDTAGQEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFVAMPALAPPEVVMDPALAAQYEHDLEVAQTTALPDEDDDL DIP protein P62826 original sequence version: 138 DIP protein P62826 original sequence version: 67 DIP protein P62826 original sequence version: 93 DIP protein P62826 original sequence version: 125 DIP protein P62826 original sequence version: 96 D5C9B7275C34BCE0 if1ax_human Eukaryotic translation initiation factor 1A, X-chromosomal Eukaryotic translation initiation factor 4C EIF1AX EIF1A EIF4C protein protein human Homo sapiens Human MPKNKGKGGKNRRRGKNENESEKRELVFKEDGQEYAQVIKMLGNGRLEAMCFDGVKRLCHIRGKLRKKVWINTSDIILVGLRDYQDNKADVILKYNADEARSLKAYGELPEHAKINETDTFGPGDDDEIQFDDIGDDDEDIDDI DIP protein P47813 original sequence version: 131 1C4209855B21BFD4 rbm8a_human RNA-binding protein 8A HSPC114 MDS014 RNA-binding motif protein 8A Ribonucleoprotein RBM8A RNA-binding protein Y14 Binder of OVCA1-1 RBM8A RBM8 protein protein human Homo sapiens Human MADVLDLHEAGGEDFAMDEDGDESIHKLKEKAKKRKGRGFGSEEGSRARMREDYDSVEQDGDEPGPQRSVEGWILFVTGVHEEATEEDIHDKFAEYGEIKNIHLNLDRRTGYLKGYTLVEYETYKEAQAAMEGLNGQDLMGQPISVDWCFVRGPPKGKRRGGRRRSRSPDRRRR 70BBD03CDDFEECFE ubc9_human SUMO-conjugating enzyme UBC9 UBE2I p18 SUMO-protein ligase UBC9 UBCE9 Ubiquitin carrier protein 9 Ubiquitin carrier protein I Ubiquitin-conjugating enzyme E2 I Ubiquitin-protein ligase I RING-type E3 SUMO transferase UBC9 protein protein human Homo sapiens Human MSGIALSRLAQERKAWRKDHPFGFVAVPTKNPDGTMNLMNWECAIPGKKGTPWEGGLFKLRMLFKDDYPSSPPKCKFEPPLFHPNVYPSGTVCLSILEEDKDWRPAITIKQILLGIQELLNEPNIQDPAQAEAYTIYCQNRVEYEKRVRAQAKKFAPS DIP protein P63279 original sequence version: 33 DIP protein P63279 original sequence version: 57 DIP protein P63279 original sequence version: 80 DIP protein P63279 original sequence version: 137 DIP protein P63279 original sequence version: 99 DIP protein P63279 original sequence version: 140 DIP protein P63279 original sequence version: 120 DIP protein P63279 original sequence version: 117 DIP protein P63279 original sequence version: 93 E2C826E9C8D0683D mgn_human Protein mago nashi homolog MAGOH MAGOHA protein protein human Homo sapiens Human MESDFYLRYYVGHKGKFGHEFLEFEFRPDGKLRYANNSNYKNDVMIRKEAYVHKSVMEELKRIIDDSEITKEDDALWPPPDRVGRQELEIVIGDEHISFTTSKIGSLIDVNQSKDPEGLRVFYYLVQDLKCLVFSLIGLHFKIKPI DIP protein P61326 original sequence version: 113 DIP protein P61326 original sequence version: 114 DIP protein P61326 original sequence version: 78 DIP protein P61326 original sequence version: 91 DIP protein P61326 original sequence version: 100 FFAD0B075E045875 eif1ax-ipo13 2 7 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 6 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 5 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified physical association physical association f1 t1 f2a f2b sf2b eif1ax-ipo13-1 4 5 weight by comassie molecular weight estimation by coomasie staining weight by comassie weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role neutral component neutral component purified purified 7 weight by comassie molecular weight estimation by coomasie staining weight by comassie weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role neutral component neutral component purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 6 weight by comassie molecular weight estimation by coomasie staining weight by comassie weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role neutral component neutral component purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain physical association physical association f2d f2e eif1ax-ipo13-2 4 7 weight by comassie molecular weight estimation by coomasie staining weight by comassie weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role neutral component neutral component purified purified 5 weight by comassie molecular weight estimation by coomasie staining weight by comassie weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction f2d f2e ipo13-eif1ax-1 3 6 weight by comassie molecular weight estimation by coomasie staining weight by comassie weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role prey prey purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 5 weight by comassie molecular weight estimation by coomasie staining weight by comassie weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role bait bait purified purified O94829:p.Asp369Arg mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain D R Wed May 02 18:11:50 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp369arg' Tue Jun 30 18:51:11 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp369Arg' tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 7 weight by comassie molecular weight estimation by coomasie staining weight by comassie weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role prey prey purified purified physical association physical association f2c Consistent with the structural analysis, reverse charge mutations of Asp369I, Asp370I, Glu436I and Asp481I to arginine in BS1 or of Arg938I to glutamate in BS2 resulted in reduction or loss of binding to eIF1A in pull-down assays (Figure 2C; Supplementary Figure 1). ipo13-eif1ax-2 3 5 weight by comassie molecular weight estimation by coomasie staining weight by comassie weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role bait bait purified purified O94829:p.Asp369_Asp370delinsArgArg mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain DD RR Thu Jul 07 12:16:51 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was asp369arg-asp370arg Fri Jul 22 11:05:45 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'asp369arg,asp370arg' Wed May 02 19:16:25 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp_asp369-370arg_arg' Tue Jun 30 19:15:39 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp369_Asp370delinsArgArg' tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 6 weight by comassie molecular weight estimation by coomasie staining weight by comassie weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role prey prey purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 7 weight by comassie molecular weight estimation by coomasie staining weight by comassie weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role prey prey purified purified physical association physical association f2c Consistent with the structural analysis, reverse charge mutations of Asp369I, Asp370I, Glu436I and Asp481I to arginine in BS1 or of Arg938I to glutamate in BS2 resulted in reduction or loss of binding to eIF1A in pull-down assays (Figure 2C; Supplementary Figure 1). ipo13-eif1ax-3 3 5 weight by comassie molecular weight estimation by coomasie staining weight by comassie weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role bait bait purified purified O94829:p.Glu436Arg mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain E R Wed May 02 17:54:36 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu436arg' Tue Jun 30 17:51:19 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Glu436Arg' tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 6 weight by comassie molecular weight estimation by coomasie staining weight by comassie weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role prey prey purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 7 weight by comassie molecular weight estimation by coomasie staining weight by comassie weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role prey prey purified purified physical association physical association f2c Consistent with the structural analysis, reverse charge mutations of Asp369I, Asp370I, Glu436I and Asp481I to arginine in BS1 or of Arg938I to glutamate in BS2 resulted in reduction or loss of binding to eIF1A in pull-down assays (Figure 2C; Supplementary Figure 1). ipo13-eif1ax-4 3 7 weight by comassie molecular weight estimation by coomasie staining weight by comassie weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role prey prey purified purified 5 weight by comassie molecular weight estimation by coomasie staining weight by comassie weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role bait bait purified purified O94829:p.[Glu436Arg;Asp481Arg] mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain E R certain certain sequence position certain certain certain sequence position certain D R Wed May 02 17:46:51 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu436arg,asp481arg' Tue Jun 30 18:40:41 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Glu436Arg;Asp481Arg]' tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 6 weight by comassie molecular weight estimation by coomasie staining weight by comassie weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role prey prey purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain physical association physical association f2c Consistent with the structural analysis, reverse charge mutations of Asp369I, Asp370I, Glu436I and Asp481I to arginine in BS1 or of Arg938I to glutamate in BS2 resulted in reduction or loss of binding to eIF1A in pull-down assays (Figure 2C; Supplementary Figure 1). ipo13-eif1ax-5 3 5 weight by comassie molecular weight estimation by coomasie staining weight by comassie weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role bait bait purified purified O94829:p.Asp481Arg mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain D R Wed May 02 18:03:03 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp481arg' Tue Jun 30 17:42:37 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp481Arg' tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 7 weight by comassie molecular weight estimation by coomasie staining weight by comassie weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role prey prey purified purified 6 weight by comassie molecular weight estimation by coomasie staining weight by comassie weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role prey prey purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain physical association physical association f2c Consistent with the structural analysis, reverse charge mutations of Asp369I, Asp370I, Glu436I and Asp481I to arginine in BS1 or of Arg938I to glutamate in BS2 resulted in reduction or loss of binding to eIF1A in pull-down assays (Figure 2C; Supplementary Figure 1). ipo13-eif1ax-6 3 7 weight by comassie molecular weight estimation by coomasie staining weight by comassie weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role prey prey purified purified 5 weight by comassie molecular weight estimation by coomasie staining weight by comassie weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role bait bait purified purified O94829:p.Arg938Glu mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain R E Wed May 02 16:17:19 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg938glu' Tue Jun 30 16:39:00 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg938Glu' tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 6 weight by comassie molecular weight estimation by coomasie staining weight by comassie weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role prey prey purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain physical association physical association f2c Consistent with the structural analysis, reverse charge mutations of Asp369I, Asp370I, Glu436I and Asp481I to arginine in BS1 or of Arg938I to glutamate in BS2 resulted in reduction or loss of binding to eIF1A in pull-down assays (Figure 2C; Supplementary Figure 1). ipo13-eif1ax-7 3 6 weight by comassie molecular weight estimation by coomasie staining weight by comassie weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role prey prey purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 5 weight by comassie molecular weight estimation by coomasie staining weight by comassie weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role bait bait purified purified tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 7 weight by comassie molecular weight estimation by coomasie staining weight by comassie weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role prey prey purified purified P47813:p.Glu30_Asp31delinsArgArg mutation disrupting mutation disrupting interaction mutation disrupting certain certain sequence position certain certain certain sequence position certain ED RR Thu Jul 07 12:15:59 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was glu30arg-asp31arg Fri Jul 22 10:51:19 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'glu30arg,asp31arg' Wed May 02 20:31:27 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu_asp30-31arg_arg' Tue Jun 30 17:59:10 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Glu30_Asp31delinsArgArg' physical association physical association f3c ipo13-eif1ax-8 3 6 weight by comassie molecular weight estimation by coomasie staining weight by comassie weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role prey prey purified purified P62826:p.[Arg95Glu;Lys130Glu] mutation disrupting mutation disrupting interaction mutation disrupting certain certain sequence position certain certain certain sequence position certain R E certain certain sequence position certain certain certain sequence position certain K E Wed May 02 19:54:01 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg95glu,lys130glu' Tue Jun 30 15:38:30 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Arg95Glu;Lys130Glu]' range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 5 weight by comassie molecular weight estimation by coomasie staining weight by comassie weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role bait bait purified purified tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 7 weight by comassie molecular weight estimation by coomasie staining weight by comassie weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role prey prey purified purified physical association physical association f3c Consistent with the structural analysis, reverse charge mutations of Asp369I, Asp370I, Glu436I and Asp481I to arginine in BS1 or of Arg938I to glutamate in BS2 resulted in reduction or loss of binding to eIF1A in pull-down assays (Figure 2C; Supplementary Figure 1). eif1ax-ipo13-3 1 5 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified 6 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 7 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified physical association physical association f3d To better understand the mechanism of the Imp13 import/export cycle, we measured the KD values by differential scanning fluorimetry (DSF) (Niesen et al, 2007) (Figure 3D; Supplementary Figure 3). The estimated KD for the two import cargoes Mago-Y14 and Ubc9 is in a similar range with a value of 235±30nM and 370±20 nM, respectively. The KD value for RanGTP binding to Imp13, although not accurately calculated due to the upper detection limit of the method, falls in the low nanomolar or picomolar range (o100 nM) and is consistent with values measured for other karyopherins (Bischoff and Go¨rlich, 1997; Deane et al, 1997; Go¨ rlich et al, 1997; Lipowsky et al, 2000). The dissociation constant of the export cargo eIF1A to a preformed Imp13-RanGTP complex is 3±0.38 mM, 10-fold higher than the KD values of the import cargoes (Figure 3D). eif1ax-ipo13-4 1 6 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 5 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified physical association physical association f3d sf3 To better understand the mechanism of the Imp13 import/export cycle, we measured the KD values by differential scanning fluorimetry (DSF) (Niesen et al, 2007) (Figure 3D; Supplementary Figure 3). The estimated KD for the two import cargoes Mago-Y14 and Ubc9 is in a similar range with a value of 235±30nM and 370±20 nM, respectively. The KD value for RanGTP binding to Imp13, although not accurately calculated due to the upper detection limit of the method, falls in the low nanomolar or picomolar range (o100 nM) and is consistent with values measured for other karyopherins (Bischoff and Go¨rlich, 1997; Deane et al, 1997; Go¨ rlich et al, 1997; Lipowsky et al, 2000). The dissociation constant of the export cargo eIF1A to a preformed Imp13-RanGTP complex is 3±0.38 mM, 10-fold higher than the KD values of the import cargoes (Figure 3D). eif1ax-ipo13-5 1 9 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified 5 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified physical association physical association f3d sf3 To better understand the mechanism of the Imp13 import/export cycle, we measured the KD values by differential scanning fluorimetry (DSF) (Niesen et al, 2007) (Figure 3D; Supplementary Figure 3). The estimated KD for the two import cargoes Mago-Y14 and Ubc9 is in a similar range with a value of 235±30nM and 370±20 nM, respectively. The KD value for RanGTP binding to Imp13, although not accurately calculated due to the upper detection limit of the method, falls in the low nanomolar or picomolar range (o100 nM) and is consistent with values measured for other karyopherins (Bischoff and Go¨rlich, 1997; Deane et al, 1997; Go¨ rlich et al, 1997; Lipowsky et al, 2000). The dissociation constant of the export cargo eIF1A to a preformed Imp13-RanGTP complex is 3±0.38 mM, 10-fold higher than the KD values of the import cargoes (Figure 3D). eif1ax-ipo13-6 1 8 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified 10 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified 5 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified physical association physical association f3d sf3 To better understand the mechanism of the Imp13 import/export cycle, we measured the KD values by differential scanning fluorimetry (DSF) (Niesen et al, 2007) (Figure 3D; Supplementary Figure 3). The estimated KD for the two import cargoes Mago-Y14 and Ubc9 is in a similar range with a value of 235±30nM and 370±20 nM, respectively. The KD value for RanGTP binding to Imp13, although not accurately calculated due to the upper detection limit of the method, falls in the low nanomolar or picomolar range (o100 nM) and is consistent with values measured for other karyopherins (Bischoff and Go¨rlich, 1997; Deane et al, 1997; Go¨ rlich et al, 1997; Lipowsky et al, 2000). The dissociation constant of the export cargo eIF1A to a preformed Imp13-RanGTP complex is 3±0.38 mM, 10-fold higher than the KD values of the import cargoes (Figure 3D). ipo13-magoh-3 3 10 weight by comassie molecular weight estimation by coomasie staining weight by comassie weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role prey prey purified purified 5 weight by comassie molecular weight estimation by coomasie staining weight by comassie weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role bait bait purified purified tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 8 weight by comassie molecular weight estimation by coomasie staining weight by comassie weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role prey prey purified purified physical association physical association f5a ipo13-magoh-4 3 5 weight by comassie molecular weight estimation by coomasie staining weight by comassie weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role bait bait purified purified tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 9 weight by comassie molecular weight estimation by coomasie staining weight by comassie weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role prey prey purified purified direct interaction direct interaction f5a ipo13-eif1ax-9 3 7 weight by comassie molecular weight estimation by coomasie staining weight by comassie weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role prey prey purified purified 6 weight by comassie molecular weight estimation by coomasie staining weight by comassie weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role prey prey purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 5 weight by comassie molecular weight estimation by coomasie staining weight by comassie weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role bait bait purified purified O94829:p.Lys802_Arg803delinsGluGlu mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain KR EE Thu Jul 07 12:17:50 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was lys802glu-arg803glu Fri Jul 22 10:53:40 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'lys802glu,arg803glu' Wed May 02 20:05:23 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys_arg802-803glu_glu' Tue Jun 30 19:09:42 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys802_Arg803delinsGluGlu' tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined physical association physical association f5a Consistent with the structural analysis, reverse charge mutations of Asp369I, Asp370I, Glu436I and Asp481I to arginine in BS1 or of Arg938I to glutamate in BS2 resulted in reduction or loss of binding to eIF1A in pull-down assays (Figure 2C; Supplementary Figure 1). Notably, an Imp13 mutant unable to bind to Mago-Y14 (Lys803Glu/Arg803GluI) is also less efficient in exporting eIF1A in vivo (Figure 4I and K), reflecting a reduction in binding to eIF1A in vitro (Figure 5A).